PDBe 2hle

X-ray diffraction
2.05Å resolution

Structural and biophysical characterization of the EPHB4-EPHRINB2 protein protein interaction and receptor specificity.

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ephrin type-B receptor 4 Chain: A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 21.35 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P54760 (Residues: 17-196; Coverage: 19%)
Gene names: EPHB4, HTK, MYK1, TYRO11
Structure domains: Galactose-binding domain-like
Ephrin-B2 Chain: B
Molecule details ›
Chain: B
Length: 138 amino acids
Theoretical weight: 15.79 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P52799 (Residues: 28-165; Coverage: 45%)
Gene names: EFNB2, EPLG5, HTKL, LERK5
Sequence domains: Ephrin
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P41
Unit cell:
a: 81.085Å b: 81.085Å c: 50.945Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.226 0.295
Expression system: Spodoptera frugiperda